| Abstract
| - Studying protein components of large intracellular complexes by in-cell NMR has so far beenimpossible because the backbone resonances are unobservable due to their slow tumbling rates. Wedescribe a methodology that overcomes this difficulty through selective labeling of methyl groups, whichpossess more favorable relaxation behavior. Comparison of different in-cell labeling schemes with threedifferent proteins, calmodulin, NmerA, and FKBP, shows that selective labeling with [13C]methyl groups onmethionine and alanine provides excellent sensitivity with low background levels at very low costs.
|
